Science Links Japan | Design and Synthesis of Heme-Binding 2.ALPHA.-Helix Peptides: Regulation of Peptide Foldings-State by Heme-Binding.

Design and Synthesis of Heme-Binding 2.ALPHA.-Helix Peptides: Regulation of Peptide Foldings-State by Heme-Binding.

Accession number;99A0228209

Title;Design and Synthesis of Heme-Binding 2.ALPHA.-Helix Peptides: Regulation of Peptide Foldings-State by Heme-Binding.

Author; SAKAMOTO SEIJI (Tokyo Inst. of Technol. Fac. of Biosci. and Biotechnol.) UENO AKIHIKO (Tokyo Inst. of Technol. Fac. of Biosci. and Biotechnol.) MIHARA HISAKAZU (Tokyo Inst. of Technol. Fac. of Biosci. and Biotechnol.)

Journal Title;Abstracts. Symposium on Biofunctional Chemistry

Journal Code:L0836A

ISSN:

VOL.13th;NO.;PAGE.61-63(1998)

Figure&Table&Reference;

Pub. Country;Japan

Language;Japanese

Abstract;We have designed and synthesized amphiphilic two-.ALPHA.-helix peptides, which bound a heme through a ligation of His residues. The peptide, H2.ALPHA.-I4 took a .BETA.-sheet structure in the buffer in the absence of heme, due to the introduction of Ile residues, which tend to form a .BETA.-sheet structure. On the other hand, in the presence of heme, the pepfide bound a heme effectively and took an .ALPHA.-helix structure in the buffer. Furthermore, the heme-binding induced a molecular assembly of peptide-heme conjugates, which was composed of 8 .ALPHA.-helices and 4 heme molecules. The heme bound to the peptide showed a strong split CD, i.e. exciton-coupling, at the Soret band, indicating that the heme molecules were highly oriented in the self-assembled peptides. These results indicated that the peptide folding-state was regulated by the heme-binding. (author abst.)

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